Evidence map›Paper›PMID 15254268›Full record

ArticleMolecular biology of the cell2004

Cell context-specific effects of the beta-tubulin glycylation domain on assembly and size of microtubular organelles.

Rupal Thazhath, Maria Jerka-Dziadosz, Jianming Duan, Dorota Wloga, Martin A Gorovsky, Joseph Frankel, Jacek Gaertig

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Anterior-posterior pattern formation in ciliates.The Journal of eukaryotic microbiology · 2022
    Review
  5. Review
  6. Article
  7. Polarity in Ciliate Models: From Cilia to Cell Architecture.Frontiers in cell and developmental biology · 2019
    Review
  8. Tubulin Post-Translational Modifications and Microtubule Dynamics.International journal of molecular sciences · 2017
    Review
  9. The Central Apparatus of Cilia and Eukaryotic Flagella.Cold Spring Harbor perspectives in biology · 2017
    Review
  10. Article
  11. Article
  12. Ciliogenesis: building the cell's antenna.Nature reviews. Molecular cell biology · 2011
    Review
  13. Article
  14. Review
  15. Article
  16. Basal body assembly in ciliates: the power of numbers.Traffic (Copenhagen, Denmark) · 2009
    Review
  17. Article
  18. Article
  19. Review
  20. Tubulin modifications and their cellular functions.Current opinion in cell biology · 2008
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Rupal ThazhathDepartment of Cellular Biology, University of Georgia, Athens, GA 30602, USA.
Maria Jerka-Dziadosz
Jianming Duan
Dorota Wloga
Martin A Gorovsky
Joseph Frankel
Jacek Gaertig
University of Georgia · USUniversity of Rochester · USInstytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLUniversity of Iowa · US

Funding

CONTROL OF GENE ACTIVITY AND ORGANELLE BIOGENESISR01GM026973 · NIGMS · UNIVERSITY OF ROCHESTER · PI GOROVSKY, MARTIN A · 1985 to 2006
$2.0M
NIGMS NIH HHS GM-026973NIGMS NIH HHS R01 GM026973
6 · The paper itself

Abstract

Tubulin glycylation is a posttranslational modification found in cells with cilia or flagella. The ciliate Tetrahymena has glycylation on ciliary and cortical microtubules. We showed previously that mutating three glycylation sites on beta-tubulin produces immotile 9 + 0 axonemes and inhibits cytokinesis. Here, we use an inducible glycylation domain mutation and epitope tagging to evaluate the potential of glycylation-deficient tubulin for assembly and maintenance of microtubular systems. In axonemes, the major defects, including lack of the central pair, occurred during assembly, and newly made cilia were abnormally short. The glycylation domain also was required for maintenance of the length of already assembled cilia. In contrast to the aberrant assembly of cilia, several types of cortical organelles showed an abnormally high number of microtubules in the same mutant cells. Thus, the consequences of deficiency in tubulin glycylation are organelle type specific and lead to either insufficient assembly (cilia) or excessive assembly (basal bodies and cortical microtubules). We suggest that the diverse functions of the beta-tubulin glycylation domain are executed by spatially restricted microtubule-associated proteins.

Indexed as

AnimalsCiliaGenes, ProtozoanGlycosylationMicroscopy, ElectronMicrotubulesMutationOrganellesPhenotypeProtein Structure, TertiaryProtozoan ProteinsTetrahymenaTubulinProtozoan ProteinsTubulin

Identifiers

PMID15254268
PMCPMC515347
OpenAlexW2006421624

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.